1VTO

1.9 A RESOLUTION REFINED STRUCTURE OF TBP RECOGNIZING THE MINOR GROOVE OF TATAAAAG

Summary for 1VTO

• Entry DOI: 10.2210/pdb1vto/pdb
• Descriptor: DNA (5'-D(*GP*CP*TP*AP*TP*AP*AP*AP*AP*GP*GP*GP*CP*A)-3'), DNA (5'-D(*TP*GP*CP*CP*CP*TP*TP*TP*TP*AP*TP*AP*GP*C)-3'), TATA BINDING PROTEIN, ... (4 entities in total)
• Functional Keywords: protein-dna complex, double helix, kinked, transcription-dna complex, transcription/dna
• Biological source: ARABIDOPSIS THALIANA (mouse-ear cress); More
• Total number of polymer chains: 6
• Total formula weight: 59853.77

Authors

Kim, J.L.,Burley, S.K. (deposition date: 1996-09-06, release date: 2011-07-13, Last modification date: 2024-03-13)

Primary citation

Kim, J.L.,Burley, S.K.
1.9 A Resolution Refined Structure of TBP Recognizing the Minor Groove of TATAAAAG
Nat.Struct.Biol., 1:638-653, 1994

PubMed Abstract: The three-dimensional structure of a TATA box-binding protein (TBP) from Arabidopsis thaliana complexed with a fourteen base pair oligonucleotide bearing the Adenovirus major late promoter TATA element has been refined at 1.9 A resolution, giving a final crystallographic R-factor of 19.4%. Binding of the monomeric, saddle-shaped alpha/beta protein induces an unprecedented conformational change in the DNA. A detailed structural and functional analysis of this unusual protein-DNA complex is presented, with particular emphasis on the mechanisms of DNA deformation, TATA element recognition, and preinitiation complex assembly.

PubMed: 7634103

Experimental method

X-RAY DIFFRACTION (1.9 Å)